ClpP1P2 peptidase activity promotes biofilm formation in Pseudomonas aeruginosa.

ABSTRACT: Caseinolytic proteases (Clp) are central to bacterial proteolysis and control cellular physiology and stress responses. They are composed of a double-ring compartmentalized peptidase (ClpP) and a AAA+ unfoldase (ClpX or ClpA/ClpC). Unlike many bacteria, the opportunistic pathogen Pseudomonas aeruginosa contains two ClpP homologs: ClpP1 and ClpP2. The specific functions of these homologs, however, are largely elusive. Here, we report that the active form of PaClpP2 is a part of a heteromeric PaClpP1₇ P2₇ tetradecamer that is required for proper biofilm development. PaClpP1₁₄ and PaClpP1₇ P2₇ complexes exhibit distinct peptide cleavage specificities and interact differentially with P. aeruginosa ClpX and ClpA. Crystal structures reveal t

SUBMITTER: Mawla GD 

PROVIDER: S-EPMC8141546 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature